› 3ucd

X-ray diffraction
1.41Å resolution

Function and Biology Details

Reaction catalysed: 
2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140553 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gamma-enolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 439 amino acids
Theoretical weight: 48.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09104 (Residues: 2-434; Coverage: 100%)
Gene name: ENO2
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 4 x MG
Ligand 2PG 1 x 2PG
Ligand PEP 1 x PEP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21212
Unit cell:
a: 105.708Å b: 118.623Å c: 67.579Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.198
Expression system: Escherichia coli

Quick links

Citations

1 review citation

When Place Matters: Shuttling of Enolase-1 Across Cellular Compartments.
Didiasova et al. (2019)
10 other articles

5 mentions without citation

SF2312 is a natural phosphonate inhibitor of enolase.
Leonard et al. (2016)
4 more